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- W2132451370 abstract "Microsomal calmodulin-stimulated ATPase (CaM- ATPase) was purified from dark-grown maize shoots by affinity chromatography and functionally reconstituted into phosphatidylcholine vesicles by detergent dialysis. The resultant proteoliposomes showed CaM- stimulated ATP hydrolysis and CaM-stimulated ATP- dependent calcium uptake, indicating that the CaMATPase is a calcium pump. Microsomal membranes prepared from dark-grown maize shoots were fractionated in continuous sucrose gradients. Calcium transport was observed in plasma membrane and intracellular membrane fractions, but the bulk of the calmodulin-stimulated activity was found to be associated with intracellular membranes. Five monoclonal antibodies were raised to affinity purified CaM- ATPase" @default.
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- W2132451370 date "1994-01-01" @default.
- W2132451370 modified "2023-09-27" @default.
- W2132451370 title "Calmodulin-stimulated ATPase of maize cells: functional reconstitution, monoclonal antibodies and subcellular localization" @default.
- W2132451370 doi "https://doi.org/10.1093/jxb/45.11.1553" @default.
- W2132451370 hasPublicationYear "1994" @default.
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